- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Zhang, L. H.
- Articles by Kolter, R.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Zhang, L. H.
- Articles by Kolter, R.
Genetics, Vol 141, 25-32, Copyright © 1995
INVESTIGATIONS |
Genetic Analysis of the Colicin V Secretion Pathway
L. H. Zhang, M. J. Fath, H. K. Mahanty, P. C. Tai and R. Kolter
Present address: Department of Immunopathology, Dana-Farber Cancer Institute, Boston, MA 02115.
Colicin V (ColV) is peptide antibiotic secreted by Escherichia coli through a dedicated exporter composed of three proteins, CvaA, CvaB, and TolC. ColV secretion is independent of the E. coli general secretory pathway (Sec) but requires an N-terminal export signal specific for the CvaAB/TolC exporter. ColV secretion was characterized using genetic and biochemical methods. When the ColV N-terminal extension is replaced with the OmpA signal sequence, the Sec system can localize ColV to the periplasm. Periplasmic ColV is lethal to cells lacking the ColV immunity protein, Cvi. Based on this result, a genetic assay was designed to monitor for the presence of periplasmic ColV during normal CvaAB/TolC mediated secretion. Results indicate that low levels of ColV may be present in the periplasm during secretion. Precursor and mature ColV were also characterized from the wild-type system and in various exporter mutant backgrounds using immunoprecipitation. ColV processing is rapid in wild-type cells, and CvaA and CvaB are critical for processing to occur. In contrast, processing occurs normally, albeit more slowly, in a TolC mutant.
This article has been cited by other articles:
 |
|
 |
|
  S. Bieler, F. Silva, C. Soto, and D. Belin Bactericidal Activity of both Secreted and Nonsecreted Microcin E492 Requires the Mannose Permease. J. Bacteriol., October 1, 2006; 188(20): 7049 - 7061. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Gerard, N. Pradel, and L.-F. Wu Bactericidal Activity of Colicin V Is Mediated by an Inner Membrane Protein, SdaC, of Escherichia coli J. Bacteriol., March 15, 2005; 187(6): 1945 - 1950. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. B. H. Shyu, D. P. Lies, and D. K. Newman Protective Role of tolC in Efflux of the Electron Shuttle Anthraquinone-2,6-Disulfonate J. Bacteriol., March 15, 2002; 184(6): 1806 - 1810. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
X. Zhong and P. C. Tai When an ATPase Is Not an ATPase: at Low Temperatures the C-Terminal Domain of the ABC Transporter CvaB Is a GTPase J. Bacteriol., March 15, 1998; 180(6): 1347 - 1353. [Abstract] [Full Text]
|
|
|
|
 |
|
 R. Srikumar, T. Kon, N. Gotoh, and K. Poole Expression of Pseudomonas aeruginosa Multidrug Efflux Pumps MexA-MexB-OprM and MexC-MexD-OprJ in a Multidrug-Sensitive Escherichia coli Strain Antimicrob. Agents Chemother., January 1, 1998; 42(1): 65 - 71. [Abstract] [Full Text]
|
|
|
|
 |
|
 K. W. Miller, R. Schamber, Y. Chen, and B. Ray Production of Active Chimeric Pediocin AcH in Escherichia coli in the Absence of Processing and Secretion Genes from the Pediococcus pap Operon Appl. Envir. Microbiol., January 1, 1998; 64(1): 14 - 20. [Abstract] [Full Text]
|
|
|
|
 |
|
 X. Zhong, R. Kolter, and P. C. Tai Processing of Colicin V-1, a Secretable Marker Protein of a Bacterial ATP Binding Cassette Export System, Requires Membrane Integrity, Energy, and Cytosolic Factors J. Biol. Chem., November 8, 1996; 271(45): 28057 - 28063. [Abstract] [Full Text] [PDF]
|
|